ES2323530T3 - Sistemas de expresion de igf recombinante. - Google Patents
Sistemas de expresion de igf recombinante. Download PDFInfo
- Publication number
- ES2323530T3 ES2323530T3 ES04755315T ES04755315T ES2323530T3 ES 2323530 T3 ES2323530 T3 ES 2323530T3 ES 04755315 T ES04755315 T ES 04755315T ES 04755315 T ES04755315 T ES 04755315T ES 2323530 T3 ES2323530 T3 ES 2323530T3
- Authority
- ES
- Spain
- Prior art keywords
- igf
- amino acids
- sequence
- terminal
- polypeptide
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 230000014509 gene expression Effects 0.000 title claims abstract description 45
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 claims abstract description 106
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 45
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 33
- 229920001184 polypeptide Polymers 0.000 claims abstract description 32
- 238000000034 method Methods 0.000 claims abstract description 19
- 150000007523 nucleic acids Chemical group 0.000 claims abstract description 13
- 108090000623 proteins and genes Proteins 0.000 claims description 64
- 150000001413 amino acids Chemical class 0.000 claims description 51
- 102000004169 proteins and genes Human genes 0.000 claims description 50
- 108091005804 Peptidases Proteins 0.000 claims description 39
- 239000004365 Protease Substances 0.000 claims description 37
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 34
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 claims description 23
- 238000003776 cleavage reaction Methods 0.000 claims description 23
- 230000007017 scission Effects 0.000 claims description 23
- 101000599951 Homo sapiens Insulin-like growth factor I Proteins 0.000 claims description 19
- 102100037852 Insulin-like growth factor I Human genes 0.000 claims description 17
- 239000013598 vector Substances 0.000 claims description 14
- 239000013604 expression vector Substances 0.000 claims description 13
- 108020004707 nucleic acids Proteins 0.000 claims description 9
- 102000039446 nucleic acids Human genes 0.000 claims description 9
- 239000000203 mixture Substances 0.000 claims description 8
- 238000002360 preparation method Methods 0.000 claims description 7
- 239000003795 chemical substances by application Substances 0.000 claims description 5
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 3
- 239000004202 carbamide Substances 0.000 claims description 3
- 230000003196 chaotropic effect Effects 0.000 claims description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 claims 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 claims 1
- 102000013275 Somatomedins Human genes 0.000 abstract description 80
- 230000004927 fusion Effects 0.000 abstract description 29
- 108020001507 fusion proteins Proteins 0.000 abstract description 8
- 102000037865 fusion proteins Human genes 0.000 abstract description 8
- 210000004027 cell Anatomy 0.000 description 58
- 108090000848 Ubiquitin Proteins 0.000 description 33
- 102000044159 Ubiquitin Human genes 0.000 description 33
- 108020004414 DNA Proteins 0.000 description 20
- 241000588724 Escherichia coli Species 0.000 description 18
- 238000004519 manufacturing process Methods 0.000 description 17
- 239000013612 plasmid Substances 0.000 description 16
- 239000000499 gel Substances 0.000 description 14
- 239000000047 product Substances 0.000 description 11
- 102000004190 Enzymes Human genes 0.000 description 10
- 108090000790 Enzymes Proteins 0.000 description 10
- 239000006142 Luria-Bertani Agar Substances 0.000 description 10
- 230000029087 digestion Effects 0.000 description 10
- 239000004098 Tetracycline Substances 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 8
- 229960002180 tetracycline Drugs 0.000 description 8
- 229930101283 tetracycline Natural products 0.000 description 8
- 235000019364 tetracycline Nutrition 0.000 description 8
- 150000003522 tetracyclines Chemical class 0.000 description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
- 238000004520 electroporation Methods 0.000 description 7
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 6
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 238000010367 cloning Methods 0.000 description 6
- 230000006698 induction Effects 0.000 description 6
- 108091008146 restriction endonucleases Proteins 0.000 description 6
- 241000894006 Bacteria Species 0.000 description 5
- 238000001502 gel electrophoresis Methods 0.000 description 5
- 229930027917 kanamycin Natural products 0.000 description 5
- 229960000318 kanamycin Drugs 0.000 description 5
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 5
- 229930182823 kanamycin A Natural products 0.000 description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 239000006137 Luria-Bertani broth Substances 0.000 description 4
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 4
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 4
- 102000035195 Peptidases Human genes 0.000 description 4
- 230000003115 biocidal effect Effects 0.000 description 4
- 238000004925 denaturation Methods 0.000 description 4
- 230000036425 denaturation Effects 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- 238000010438 heat treatment Methods 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 102000012410 DNA Ligases Human genes 0.000 description 3
- 108010061982 DNA Ligases Proteins 0.000 description 3
- 101800001491 Protease 3C Proteins 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 238000000246 agarose gel electrophoresis Methods 0.000 description 3
- 230000015556 catabolic process Effects 0.000 description 3
- 230000006037 cell lysis Effects 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 238000006731 degradation reaction Methods 0.000 description 3
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 3
- 230000013011 mating Effects 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 239000013049 sediment Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 229920000936 Agarose Polymers 0.000 description 2
- 241000206602 Eukaryota Species 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- 241000710122 Rhinovirus B14 Species 0.000 description 2
- 108010006785 Taq Polymerase Proteins 0.000 description 2
- 238000005273 aeration Methods 0.000 description 2
- 239000000556 agonist Substances 0.000 description 2
- 229960000723 ampicillin Drugs 0.000 description 2
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 2
- 230000001195 anabolic effect Effects 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 210000000805 cytoplasm Anatomy 0.000 description 2
- 239000008367 deionised water Substances 0.000 description 2
- 229910021641 deionized water Inorganic materials 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 238000011194 good manufacturing practice Methods 0.000 description 2
- 102000044162 human IGF1 Human genes 0.000 description 2
- 210000003000 inclusion body Anatomy 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 229910001629 magnesium chloride Inorganic materials 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 238000006116 polymerization reaction Methods 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- 108010091324 3C proteases Proteins 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 108010013369 Enteropeptidase Proteins 0.000 description 1
- 102100029727 Enteropeptidase Human genes 0.000 description 1
- 241000672609 Escherichia coli BL21 Species 0.000 description 1
- 241001302584 Escherichia coli str. K-12 substr. W3110 Species 0.000 description 1
- 108010074860 Factor Xa Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101100452299 Homo sapiens IGF1 gene Proteins 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- OLWAOWXIADGIJG-AVGNSLFASA-N Met-Arg-Lys Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(O)=O OLWAOWXIADGIJG-AVGNSLFASA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000003042 antagnostic effect Effects 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000000326 densiometry Methods 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000009210 therapy by ultrasound Methods 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/65—Insulin-like growth factors, i.e. somatomedins, e.g. IGF-1, IGF-2
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Gastroenterology & Hepatology (AREA)
- Endocrinology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Toxicology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Diabetes (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US47794103P | 2003-06-13 | 2003-06-13 | |
| US477941P | 2003-06-13 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2323530T3 true ES2323530T3 (es) | 2009-07-20 |
Family
ID=33539073
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES04755315T Expired - Lifetime ES2323530T3 (es) | 2003-06-13 | 2004-06-14 | Sistemas de expresion de igf recombinante. |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US7354994B2 (de) |
| EP (1) | EP1646650B9 (de) |
| JP (1) | JP2007530010A (de) |
| AT (1) | ATE429446T1 (de) |
| CA (1) | CA2529282C (de) |
| DE (1) | DE602004020771D1 (de) |
| ES (1) | ES2323530T3 (de) |
| PL (1) | PL1646650T3 (de) |
| WO (1) | WO2004113382A1 (de) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102586257A (zh) * | 2012-01-20 | 2012-07-18 | 吉林农业大学 | 梅花鹿igf-1多肽及其制备方法 |
| JP2020156412A (ja) * | 2019-03-27 | 2020-10-01 | 三菱ケミカル株式会社 | 改変されたプロテアーゼ切断配列を含むアクチビンａ |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6068994A (en) * | 1989-08-07 | 2000-05-30 | Chiron Corporation | Ubiquitin expression system |
| US5563046A (en) * | 1993-08-02 | 1996-10-08 | Celtrix Pharmaceuticals, Inc. | Fusion polypeptides and proteins |
| US5861273A (en) | 1993-12-21 | 1999-01-19 | Celtrix Phamraceuticals, Inc. | Chromosomal expression of heterologous genes in bacterial cells |
| US5470727A (en) * | 1993-12-21 | 1995-11-28 | Celtrix Pharmaceuticals, Inc. | Chromosomal expression of non-bacterial genes in bacterial cells |
| JP4088584B2 (ja) * | 2001-07-26 | 2008-05-21 | アドバンスド プロテイン テクノロジーズ コーポレイション | 融合タンパク質から目的タンパク質を分離する方法。 |
-
2004
- 2004-06-14 ES ES04755315T patent/ES2323530T3/es not_active Expired - Lifetime
- 2004-06-14 DE DE602004020771T patent/DE602004020771D1/de not_active Expired - Lifetime
- 2004-06-14 WO PCT/US2004/019070 patent/WO2004113382A1/en not_active Ceased
- 2004-06-14 AT AT04755315T patent/ATE429446T1/de active
- 2004-06-14 PL PL04755315T patent/PL1646650T3/pl unknown
- 2004-06-14 CA CA2529282A patent/CA2529282C/en not_active Expired - Lifetime
- 2004-06-14 EP EP04755315A patent/EP1646650B9/de not_active Expired - Lifetime
- 2004-06-14 US US10/866,086 patent/US7354994B2/en not_active Expired - Lifetime
- 2004-06-14 JP JP2006533801A patent/JP2007530010A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| EP1646650B1 (de) | 2009-04-22 |
| CA2529282A1 (en) | 2004-12-29 |
| WO2004113382A1 (en) | 2004-12-29 |
| US7354994B2 (en) | 2008-04-08 |
| JP2007530010A (ja) | 2007-11-01 |
| CA2529282C (en) | 2013-05-28 |
| DE602004020771D1 (de) | 2009-06-04 |
| EP1646650A1 (de) | 2006-04-19 |
| ATE429446T1 (de) | 2009-05-15 |
| EP1646650B9 (de) | 2010-02-03 |
| HK1089457A1 (en) | 2006-12-01 |
| US20050095672A1 (en) | 2005-05-05 |
| PL1646650T3 (pl) | 2009-09-30 |
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